ID   NTE1_EREGS              Reviewed;        1522 AA.
AC   Q756Z0;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   24-JAN-2024, entry version 114.
DE   RecName: Full=Lysophospholipase NTE1;
DE            EC=3.1.1.5;
DE   AltName: Full=Intracellular phospholipase B;
DE   AltName: Full=Neuropathy target esterase homolog;
GN   Name=NTE1; OrderedLocusNames=AER124W;
OS   Eremothecium gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL
OS   Y-1056) (Yeast) (Ashbya gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- FUNCTION: Intracellular phospholipase B that catalyzes the double
CC       deacylation of phosphatidylcholine (PC) to glycerophosphocholine
CC       (GroPCho). Plays an important role in membrane lipid homeostasis.
CC       Responsible for the rapid PC turnover in response to inositol, elevated
CC       temperatures, or when choline is present in the growth medium (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid +
CC         H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870,
CC         ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5;
CC   -!- ACTIVITY REGULATION: Inhibited by organophosphorus esters.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC       Single-pass type I membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the NTE family. {ECO:0000305}.
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DR   EMBL; AE016818; AAS52807.1; -; Genomic_DNA.
DR   RefSeq; NP_984983.1; NM_210337.1.
DR   AlphaFoldDB; Q756Z0; -.
DR   SMR; Q756Z0; -.
DR   STRING; 284811.Q756Z0; -.
DR   EnsemblFungi; AAS52807; AAS52807; AGOS_AER124W.
DR   GeneID; 4621189; -.
DR   KEGG; ago:AGOS_AER124W; -.
DR   eggNOG; KOG2968; Eukaryota.
DR   HOGENOM; CLU_000960_1_1_1; -.
DR   InParanoid; Q756Z0; -.
DR   OMA; SSGYVWR; -.
DR   OrthoDB; 5303733at2759; -.
DR   Proteomes; UP000000591; Chromosome V.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004622; F:lysophospholipase activity; IBA:GO_Central.
DR   GO; GO:0102545; F:phosphatidyl phospholipase B activity; IEA:UniProtKB-EC.
DR   GO; GO:0034638; P:phosphatidylcholine catabolic process; IEA:EnsemblFungi.
DR   GO; GO:0071071; P:regulation of phospholipid biosynthetic process; IEA:EnsemblFungi.
DR   CDD; cd00038; CAP_ED; 2.
DR   Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 2.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 3.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR018490; cNMP-bd_dom_sf.
DR   InterPro; IPR001423; LysoPLipase_patatin_CS.
DR   InterPro; IPR002641; PNPLA_dom.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   PANTHER; PTHR14226:SF29; NEUROPATHY TARGET ESTERASE SWS; 1.
DR   PANTHER; PTHR14226; NEUROPATHY TARGET ESTERASE/SWISS CHEESE D.MELANOGASTER; 1.
DR   Pfam; PF00027; cNMP_binding; 2.
DR   Pfam; PF01734; Patatin; 1.
DR   SMART; SM00100; cNMP; 2.
DR   SUPFAM; SSF51206; cAMP-binding domain-like; 3.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   PROSITE; PS50042; CNMP_BINDING_3; 2.
DR   PROSITE; PS51635; PNPLA; 1.
DR   PROSITE; PS01237; UPF0028; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; Hydrolase; Lipid degradation; Lipid metabolism;
KW   Membrane; Reference proteome; Repeat; Transmembrane; Transmembrane helix.
FT   CHAIN           1..1522
FT                   /note="Lysophospholipase NTE1"
FT                   /id="PRO_0000295308"
FT   TOPO_DOM        1..73
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        74..94
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        95..1522
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   DOMAIN          1219..1383
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   REGION          443..468
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          485..523
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          535..556
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          828..852
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1125..1145
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           1223..1228
FT                   /note="GXGXXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOTIF           1250..1254
FT                   /note="GXSXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOTIF           1370..1372
FT                   /note="DGA/G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   COMPBIAS        485..519
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        535..551
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1252
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   ACT_SITE        1370
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   BINDING         661..782
FT                   /ligand="a nucleoside 3',5'-cyclic phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58464"
FT                   /ligand_label="1"
FT   BINDING         778..918
FT                   /ligand="a nucleoside 3',5'-cyclic phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58464"
FT                   /ligand_label="2"
SQ   SEQUENCE   1522 AA;  170071 MW;  9013C45B4D219D27 CRC64;
     MVDGTYVNSS VEAISGEADT AAVAELANQM VMNFLYESSS WLAQSTGPFL WKGFRFLFLR
     LPSSLLVYLI NGTVPFYLVV LGSVFTPIIV YLILRSRVLS AYSRLKGDNE DEVIDKKKQL
     VNDSEAMLMG GPDGKRRSGF SSYLDEFLSA IKIFGYLDKL VFHELTKSMR TQRLEQGEVM
     LLDDSVGFAI VVEGGLHIYH KIAHSQGSTR ESMPLPEDRS FDSNEDDLTI NGERFQLLNK
     VKAGNPVSSL VSILKLFTDN HTPTVVDSSK SSPKQSAQVP IRQLISPFLD GNVERNKATL
     NMKQVPTAEY EIPSAERAGS NVSSFTQQLY ESMLPKDHAA EDVREPLPEI VAYAASDCAI
     AVIPASSFKR LMVKYPRSAS QIIQVILTKL YRVTFQTAHS YLGLTKEIMH TEVVLNNSTN
     FELPYYLQEA ILRKIKNGSK ESSVQESIHR ATLRSKNVHA HNSPTPNKIS RHIALESRDQ
     YNPGDLLSNV PLSRKGSKTA SSSSVSIPRI SSLRHQKEAA SSPLATLRRL EGNDSQNFAP
     LSSSSPMSVS EKPSVVGGGA HDNISQISFS SALEETEESS WRMALVESMF GYLGITNESI
     MPPTEDLLFL NNRASSGSSV CSVSSYSHPQ TINQDLFRCL SPELVRTKKK APRQKYTEEM
     PINVDFNTAK EEFAEGLETL FIPSGATIVE QNGNNKGLYY IVSGELLVCW KNEEDNIEYV
     LYTVKPGGIA GYLASLIGFK SFVSLRAKTD LYVGFLPIEV LERLCDKYFM IYLKIAETLT
     KLLSPKILKL DYALEWIHLE ASETLFNQND PANAIYVVLN GRLRQLHQKS KNEERLSRPT
     TQRKKRKDDN QPNVQVVGEY SQGCSFGEVE VLTAMNRVST VVAVRDTELA RIPRTLFEVL
     ALEHPSIMIR VSRLVAHKIL QRSSDIREPT KIVNSANGYR YDFNLTIPPS AGTSSWGNNS
     DGGSISYKTI TILPITYGLP VEEFANKLVS TFRQVGRSTI GLTQCTTLKH LGRHAFDKLA
     NLKQSGYFAE LEELYELVVY IADTPVKSSW TSTCISQGDC ILLLADASSD PEIGEFERLL
     INNRTTARTE LLLLHPERYV EPGLTHKWLR KRTWVHQHHH MQFVSSQNPS ERVDSKAPPI
     PGAPPNLIGR LKKRERLNQL TKRTQENFAR LLPDSIKLTV ENISMKYIQK KQKYYTPVSA
     HKNDFLRLAR ILSGQAIGLV LGGGGARGIS HLGILKAIEE HGIPIDMIGG TSIGSFVGGL
     YAKDYDLVPT YGRVKKFAGR IGSIWRMLSD LTWPVTSYTT GHEFNRGIWK AFGDIRIEDF
     WIQYYCNSTN ITESMQEIHT FGYAWRYVRA SMSLAGILPP ITDNGNMLLD GGYLDNLPVL
     EMKARGCKTI FAVDVGSVDD RTPMDYGDSL NGFWIVLNRW NPFSKHPNVP SMAEIQMRLG
     YVASVNALEK AKTTQGVVYF RPPIEDYATL DFAKFEEIYQ VGTAYGATFL HELEQNGKLP
     RIPGNEPANG PGIHLLHRRN SI
//